This project is comprised of research into the structure and function of ion transport systems. There are currently three active subprojects: 1) Transient kinetics: A collaborative study with Froehlich and Fendler. The source of the transmembrane current that is generated by phosphorylation of the sodium pump has been identified as either the major conformational transition or the dissociation of Na+ that immediately succeeds this event, 2) Studies of the sodium selectivity of different stages of the sodium pump mechanism. Steady-state phosphorylation kinetics have been employed to identify a role for Mg2+ in establishing the sodium selectivity of the ionophoric domain of the sodium pump and to correlate this with the conformational state of the pump; and 3) Expression and localization of sodium pump isoforms in the nervous system. A study of the regulation and expression of isoforms of the Na,K- ATPase utilizing oligonucleotides and site-directed antibodies (raised against synthetic peptides as identifying probes.

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Intramural Research (Z01)
Project #
1Z01NS000813-31
Application #
3846141
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
31
Fiscal Year
1992
Total Cost
Indirect Cost
City
State
Country
United States
Zip Code
Rudrabhatla, Parvathi; Zheng, Ya-Li; Amin, Niranjana D et al. (2008) Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein. J Biol Chem 283:26737-47
Amin, Niranjana D; Zheng, Ya-Li; Kesavapany, Sashi et al. (2008) Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis. J Neurosci 28:3631-43
Kesavapany, Sashi; Patel, Vyomesh; Zheng, Ya-Li et al. (2007) Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons. Mol Biol Cell 18:3645-55
Mahaney, James E; Albers, R Wayne; Waggoner, Jason R et al. (2005) Intermolecular conformational coupling and free energy exchange enhance the catalytic efficiency of cardiac muscle SERCA2a following the relief of phospholamban inhibition. Biochemistry 44:7713-24
Mahaney, James E; Albers, R Wayne; Kutchai, Howard et al. (2003) Phospholamban inhibits Ca2+ pump oligomerization and intersubunit free energy exchange leading to activation of cardiac muscle SERCA2a. Ann N Y Acad Sci 986:338-40
Amin, Niranjana D; Albers, Wayne; Pant, Harish C (2002) Cyclin-dependent kinase 5 (cdk5) activation requires interaction with three domains of p35. J Neurosci Res 67:354-62
Zheng, Ya-Li; Li, Bing-Sheng; Amin, Niranjana D et al. (2002) A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells. Eur J Biochem 269:4427-34